6LBF: FEM1B

Crystal structure of FEM1B. Determined by X-ray diffraction at 3.25 Å resolution. Released 21 Oct 2020.

Method: X-ray diffraction
Resolution: 3.25 Å
Organism: Homo sapiens
Chains: 2
Atoms: 5,094
Mol. weight: 79.11 kDa
Released: 21 Oct 2020

Explore 6LBF in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6LBF contains 42 α-helices and 10 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 21 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	2-14	13
α-helix	17-24	8
α-helix	29-37	9
β-strand	40-41	2	1
β-strand	46-47	2	1
α-helix	49-55	7
α-helix	59-68	10
β-strand	76-81	6	1
β-strand	84-90	7	1
α-helix	91-98	8
α-helix	101-109	9
α-helix	124-131	8
α-helix	134-142	9
α-helix	157-164	8
α-helix	167-175	9
α-helix	190-197	8
α-helix	200-208	9
α-helix	222-228	7
α-helix	232-239	8
α-helix	247-259	13
α-helix	269-283	15
α-helix	295-299	5
α-helix	306-308	3
α-helix	311-315	5
α-helix	321-335	15

Chain B: 21 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	3-14	12
α-helix	17-23	7
α-helix	29-37	9
β-strand	40-41	2	2
β-strand	46-47	2	2
α-helix	49-55	7
α-helix	59-69	11
β-strand	76-80	5	3
β-strand	85-90	6	3
α-helix	91-97	7
α-helix	101-109	9
α-helix	124-131	8
α-helix	134-142	9
α-helix	157-164	8
α-helix	167-174	8
β-strand	183	1	4
β-strand	189	1	4
α-helix	190-197	8
α-helix	200-208	9
α-helix	222-228	7
α-helix	232-239	8
α-helix	246-259	14
α-helix	270-284	15
α-helix	295-297	3
α-helix	306-308	3
α-helix	311-315	5
α-helix	321-335	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein fem-1 homolog B	A, B	protein	356	Homo sapiens	Q9UK73 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6LBF_1 Protein fem-1 homolog B (chains A, B)
MEGLAGYVYKAASEGKVLTLAALLLNRSESDIRYLLGYVSQQGGQRSTPLIIAARNGHAK
VVRLLLEHYRVQTQQTGTVRFDGYVIDGATALWCAAGAGHFEVVKLLVSHGANVNHTTVT
NSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRADP
NAKAHCGATALHFAAEAGHIDIVKELIKWRAAIVVNGHGMTPLKVAAESCKADVVELLLS
HADCDRRSRIEALELLGASFANDRENYDIIKTYHYLYLAMLERFQDGDNILEKEVLPPIH
AYGNRTECRNPQELESIRQDRDALHMEGLIVRERILGADNIDVSHPIIYRGAVYAD

Primary citation

Molecular basis for arginine C-terminal degron recognition by Cul2 FEM1 E3 ligase. Chen, X., Liao, S., Makaros, Y. et al. Nat Chem Biol (2021) 17:254-262. DOI 10.1038/s41589-020-00704-3 · PubMed

Other PDB entries of the same protein (UniProt Q9UK73 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9PW8 2.8 Å, Fem-1 homolog B (FEM1B) in complex with VU0417412
7EL6 2.8 Å, Structure of SMCR8 bound FEM1B
9PQA 2.9 Å, Fem-1 homolog B (FEM1B) in complex with VU0432623
9PQ9 2.93 Å, Fem-1 homolog B (FEM1B) in complex with VU0421763
9PWJ 3.0 Å, Fem-1 homolog B (FEM1B) in complex with VU0081201
9PXP 3.0 Å, Fem-1 homolog B (FEM1B) in complex with VU0416476
9PXO 3.05 Å, Fem-1 homolog B (FEM1B) in complex with VU0023775
9PQE 3.1 Å, Fem-1 homolog B (FEM1B) in complex with VU0412674
8WQF 3.27 Å, cryo-EM structure of CUL2-RBX1-ELOB-ELOC-FEM1B bound with the C-degron of CUX1…
8WQB 3.37 Å, Cryo-EM structure of CUL2-RBX1-ELOB-ELOC-FEM1B bound with the C-degron of CCDC89…
8WQE 3.38 Å, Cryo-EM structure of CUL2-RBX1-ELOB-ELOC-FEM1B bound with the C-degron of CUX1…
8WQA 3.39 Å, Cryo-EM structure of CUL2-RBX1-ELOB-ELOC-FEM1B bound with the C-degron of CCDC89…

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